Hemagglutinating activity and conformation of a lactose-binding lectin from mushroom Agrocybe cylindracea

Liu, Chao; Zhao, Xuelin; Xu, Xiao-Chao; Li, Lingrui; Liu, Yanhong; Zhong, Shao-Dong; Bao, Ji

doi:10.1016/j.ijbiomac.2007.10.017

Cited by 19 publications

(5 citation statements)

References 29 publications

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“…Homodimer 2 Gal-β1,4-GlcNAc na nd (Ban et al 2005;Imamura et al 2011;Kuwabara et al 2013;Liu et al 2008;Yagi et al 2001;Yagi et al 1997) Neu5Ac-α2,3-Gal-β1,4-…”

Section: Galectin (1ww7)mentioning

confidence: 99%

Entomotoxic and nematotoxic lectins and protease inhibitors from fungal fruiting bodies

Sabotič

Ohm

Künzler

2015

Appl Microbiol Biotechnol

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Fruiting bodies or sporocarps of dikaryotic (ascomycetous and basidiomycetous) fungi, commonly referred to as mushrooms, are often rich in entomotoxic and nematotoxic proteins that include lectins and protease inhibitors. These protein toxins are thought to act as effectors of an innate defense system of mushrooms against animal predators including fungivorous insects and nematodes. In this review, we summarize current knowledge about the structures, target molecules, and regulation of the biosynthesis of the best characterized representatives of these fungal defense proteins, including galectins, beta-trefoil-type lectins, actinoporin-type lectins, beta-propeller-type lectins and beta-trefoil-type chimerolectins, as well as mycospin and mycocypin families of protease inhibitors. We also present an overview of the phylogenetic distribution of these proteins among a selection of fungal genomes and draw some conclusions about their evolution and physiological function. Finally, we present an outlook for future research directions in this field and their potential applications in medicine and crop protection.

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“…Homodimer 2 Gal-β1,4-GlcNAc na nd (Ban et al 2005;Imamura et al 2011;Kuwabara et al 2013;Liu et al 2008;Yagi et al 2001;Yagi et al 1997) Neu5Ac-α2,3-Gal-β1,4-…”

Section: Galectin (1ww7)mentioning

confidence: 99%

Entomotoxic and nematotoxic lectins and protease inhibitors from fungal fruiting bodies

Sabotič

Ohm

Künzler

2015

Appl Microbiol Biotechnol

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“…Treating purified OPA with NBS, a reagent specific for Trp residues in restricted conditions, resulted in a 27% drop in the activity of OPA, which suggested the partial necessity of Trp residues for the activity of OPA. It might be located on surface or the shallow grooves of the molecule since tryptophan could be modified completely without denaturant [47]. It was an evident that an obvious decrease and blue shift (from 340 nm to 330 nm) of the fluorescence emission spectrum were observed with the increase of NBS concentration, which showed that the tryptophan residue of OPA located in hydrophobic areas on the surface of the molecule or the indole rings of tryptophan residue might be in special conformation [48].…”

Section: Discussionmentioning

confidence: 99%

Purification, Characterization, and Molecular Cloning of a Novel Antifungal Lectin From the Roots of Ophioglossum pedunculosum

Xiang

et al. 2011

Appl Biochem Biotechnol

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A novel mannan-specific lectin was isolated from the roots of a traditional Chinese herbal medicine, Ophioglossum pedunculosum through ion-exchange chromatography and gel filtration. With a molecular mass of 19,835.7 Da demonstrated by MALDI-TOF analysis, this novel agglutinin was designated as O. pedunculosum agglutinin (OPA), specifically agglutinating human O erythrocytes and rabbit erythrocytes. The hemagglutination could be strongly inhibited by mannan and thyroglobulin, the activity of which was stable in pH range of 4.0-8.0 and at temperatures below 50 °C. Chemical modification studies indicated that tryptophan and arginine residues were essential for its hemagglutinating activity. Meanwhile, it showed antifungal activities toward Sclerotium rolfsii and Fusarium graminearum. In addition, to amplify cDNA of OPA by 3'/5'-rapid amplification of cDNA ends (RACE), the N-terminal 30 amino acids sequence of OPA was determined, and degenerate primers were designed. The obtained full-length cDNA of OPA contained 885 bp with an open-reading frame of 600 bp encoding a precursor protein of 199 amino acids, while the mature protein had 170 amino acids.

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“…A. aegerita Lectin was relatively stable, had good activity at 60 °C, and could still maintain activity in extremely acidic (pH 2.42) or extremely alkaline (pH 12.22) environments, which was relatively rare among lectin (Sun et al 2003 ). The primary structure of A. cylindracea lectin was similar to that of fungal galectins, with 37% sequence homology to Coprinus galectins and only 19% sequence homology to human galectin-1 (Yagi et al 2001 ; Liu et al 2008 ).…”

Section: Lectinsmentioning

confidence: 99%

A comprehensive review of secondary metabolites from the genus Agrocybe : Biological activities and pharmacological implications

Zhang,

Yan,

Liu

2023

Mycology

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The genus Agrocybe , situated within the Strophariaceae family, class Agaricomycetes, and phylum Basidiomycota, encompasses a myriad of species exhibiting significant biological activities. This review presents an integrative overview of the secondary metabolites derived from Agrocybe species, elucidating their respective biological activities and potential pharmacological applications. The metabolites under scrutiny encompass a diverse array of biological macromolecules, specifically polysaccharides and lectins, as well as a diverse group of 80 documented small molecular chemical constituents, classified into sterols, sesquiterpenes, volatile compounds, polyenes, and other compounds, their manifesting anti-inflammatory, anticancer, antioxidant, hepatoprotective, antimicrobial, and antidiabetic activities, these metabolites, in which polysaccharides exhibit abundant activities, underscore the potential of the Agrocybe genus as a valuable source of biologically active natural products. The present review emphasises the need for escalated research into Agrocybe , including investigations into the biosynthetic pathways of these metabolites, which could foster the development of novel pharmaceutical therapies to address various health challenges.

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Hemagglutinating activity and conformation of a lactose-binding lectin from mushroom Agrocybe cylindracea

Cited by 19 publications

References 29 publications

Entomotoxic and nematotoxic lectins and protease inhibitors from fungal fruiting bodies

Entomotoxic and nematotoxic lectins and protease inhibitors from fungal fruiting bodies

Purification, Characterization, and Molecular Cloning of a Novel Antifungal Lectin From the Roots of Ophioglossum pedunculosum

A comprehensive review of secondary metabolites from the genus Agrocybe : Biological activities and pharmacological implications

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